We expect a complete 95% of the sequencing on porcine aortic tropoelastin within the coming year. Solid state amino acid sequencing has proven highly amenable and compatable with the tropoelastin peptides which are very hydrophobic. In addition to this high precision liquid chromatography has allowed identification of all the PTH amino acids and their exact quantation. We expect to achieve successful application of a Dintzes-type experiment to be used in the ordering of the tryptic fragments. A highly efficient system for production of elastin and tropoelastin has been developed with cultured fetal rat smooth muscle cells.